ArticleJournal of chemical theory and computation2021
Association Mechanism of Peptide-Coated Metal Nanoparticles with Model Membranes: A Coarse-Grained Study.
Article in Journal of chemical theory and computation, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed.
- Influence of branched ligand architectures on nanoparticle interactions with lipid bilayers.Nanoscale · 2025Article
- Translocation of TiRSC advances · 2024Article
- Inter-Organelle Contact Sites Mediate the Intracellular Antioxidant Activity of Platinum Nanozymes: A New Perspective on Cell-Nanoparticle Interaction and Signaling.ACS applied materials & interfaces · 2023Article
- Towards design of drugs and delivery systems with the Martini coarse-grained model.QRB discovery · 2022Review
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5 authors.
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Abstract
Functionalized metal nanoparticles (NPs) hold great promise as innovative tools in nanomedicine. However, one of the main challenges is how to optimize their association with the cell membrane, which is critical for their effective delivery. Recent findings show high cellular uptake rates for NPs coated with the polycationic cell-penetrating peptide gH625-644 (gH), although the underlying internalization mechanism is poorly understood. Here, we use extended coarse-grained simulations and free energy calculations to study systems that simultaneously include metal NPs, peptides, lipids, and sterols. In particular, we investigate the first encounter between multicomponent model membranes and 2.5 nm metal NPs coated with gH (gHNPs), based on the evidence from scanning transmission electron microscopy. By comparing multiple membrane and (membranotropic) NP models, we found that gHNP internalization occurs by forming an intermediate state characterized by specific stabilizing interactions formed by peptide-coated nanoparticles with multicomponent model membranes. This association mechanism is mainly characterized by interactions of gH with the extracellular solvent and the polar membrane surface. At the same time, the NP core interacts with the transmembrane (cholesterol-rich) fatty phase.
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